1URS
X-ray structures of the maltose-maltodextrin binding protein of the thermoacidophilic bacterium Alicyclobacillus acidocaldarius
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 49.180, 70.530, 104.060 |
Unit cell angles | 90.00, 96.98, 90.00 |
Refinement procedure
Resolution | 40.000 - 1.450 |
R-factor | 0.21 |
Rwork | 0.210 |
R-free | 0.23200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1urg |
RMSD bond length | 0.005 |
RMSD bond angle | 1.210 |
Data reduction software | XDS (V. 2002) |
Data scaling software | XDS (V. 2002) |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.140 | 1.500 |
High resolution limit [Å] | 1.450 | 1.450 |
Rmerge | 0.084 * | 0.509 |
Number of reflections | 137804 | |
<I/σ(I)> | 12.7 | 2.4 |
Completeness [%] | 99.6 | 98.7 |
Redundancy | 6.2 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 7.2 * | 18 * | PEG 8000, CHES, PH 9.5, 10% GLYCEROL |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 9.6 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 50 (mM) | pH7.2 |
3 | 1 | drop | glycerol | 5 (%) | |
4 | 1 | drop | maltose | 10 (mM) | |
5 | 1 | reservoir | PEG8000 | 20 (%(w/v)) | |
6 | 1 | reservoir | CHES | 100 (mM) | pH9.5 |